Proteomics

Dataset Information

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Identification of phosphorylation sites in human IGF2BP1 by immunoprecipitation coupled to mass spectrometry


ABSTRACT: Many RNA-binding proteins are regulated by posttranslational modifications, most commonly phosphorylation. IGF2BP1 is an RNA-binding protein, which regulates protein stability, translation and localization. Moreover, it was proposed to regulate mRNA stability and translation during proteotoxic stress. Here, we used immunoprecipitation coupled to mass spectrometry to identify phosphorylation sites in IGF2BP1 under control conditions and under conditions where mammalian cells were subjected to proteotoxic stress.

INSTRUMENT(S): Q Exactive HF-X

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: David Hollenstein  

LAB HEAD: Gülsün Elif Karagöz

PROVIDER: PXD045761 | Pride | 2024-11-13

REPOSITORIES: Pride

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Publications

IGF2BP1 phosphorylation in the disordered linkers regulates ribonucleoprotein condensate formation and RNA metabolism.

Hornegger Harald H   Anisimova Aleksandra S AS   Muratovic Adnan A   Bourgeois Benjamin B   Spinetti Elena E   Niedermoser Isabell I   Covino Roberto R   Madl Tobias T   Karagöz G Elif GE  

Nature communications 20241020 1


The insulin-like growth factor 2 mRNA binding protein 1 (IGF2BP1) is a conserved RNA-binding protein that regulates RNA stability, localization and translation. IGF2BP1 is part of various ribonucleoprotein (RNP) condensates. However, the mechanism that regulates its assembly into condensates remains unknown. By using proteomics, we demonstrate that phosphorylation of IGF2BP1 at S181 in a disordered linker is regulated in a stress-dependent manner. Phosphomimetic mutations in two disordered linke  ...[more]

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